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Article

Protein stability models fail to capture epistatic interactions of double point mutations

2024-08-21

Abstract excerpt

There is strong interest in accurate methods for predicting changes in protein stability resulting from amino acid mutations to the protein sequence. Recombinant proteins must often be stabilized to be used as therapeutics or reagents, and destabilizing mutations are implicated in a variety of diseases. Due to increased data availability and improved modeling techniques, recent studies have shown advancements in p...

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Identifiers and source

Literature Corpus work
918a314c-e2c8-5f68-b3d5-9cca40db8719
DOI
10.1101/2024.08.20.608844
Open publication

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Protein stability models fail to capture epistatic interactions of double point mutationsDOI 10.1101/2024.08.20.608844
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